By R. John Mayer, Aaron J. Ciechanover, Martin Rechsteiner
This sequence of 4 topical volumes comprises greater than 50 contributions protecting all features of the molecular biology and body structure of managed protein breakdown in better organisms through the ubiquitin-proteasome pathway. The editors and authors contain nearly all of the best scientists within the box, together with the pioneers of protein degradation study and the 2004 Nobel laureate in chemistry.
every one quantity highlights a unique point of the sphere, particularly ubiquitin and the chemistry of lifestyles, in addition to the mobile biology and pathology of the ubiquitin-proteasome method, with the person volumes that includes their very own separate indices. jointly, all 4 volumes give you the so much finished reference on protein degradation on hand.
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Additional resources for Protein Degradation, Volume 1: Ubiquitin and the Chemistry of Life
Sample text
IscS mobilizes sulfur from cysteine forming an IscS persulfide that is subsequently shuttled to ThiI, a rhodanese-like enzyme, to form a putative ThiI persulfide. This moiety is responsible for attacking the ThiS adenylate, which is bound at the ThiF active site, leading to the formation of the thiocarboxylate product. IscS has also been implicated in Moco biosynthesis together with the related CSD protein [29], although ThiI is not involved. It is interesting to note that some MoeB orthologs, including human MoeB, contain an additional C-terminal domain, which shares distant sequence relationships with rhodaneses.
B) Side-by-side comparison of MoaD (yellow) and ubiquitin (red) in the same orientation. (C) Stereo diagram of a leastsquares superposition of MoaD (yellow) and ubiquitin (red). 3 Structural Studies of the MoeB–MoaD Complex elements, a five-stranded mixed b-sheet packed against an a-helix, which runs diagonally across one face of the b-sheet, are present in both structures and also in ThiS. However, there is no statistically meaningful level of sequence conservation between MoaD and ubiquitin (7% identity) with the exception of the C-terminal Gly–Gly dipeptide.
And Ballard, D. W. Signal-induced degradation of IkBa requires site-specific ubiquitina˙ tion. Proc. Natl Acad. Sci. USA, 1995, 92, 11259–11263. , Kulka, R. G. and Fink, G. R. Regulated degradation of the transcription factor Gcn4. , 1994, 13, 6021–6030. Sokolik, C. W. and Cohen, R. E. The structures of ubiquitin conjugates of yeast Iso-2-cytochrome c. J. Biol. , 1991, 266, 9100–9107. , Tobias, J. , Ecker, D. , Gonda, D. K. and Varshavsky, A. A multi ubiquitin chain is confined to specific lysine in a targeted short-lived protein.